The c-Abl nonreceptor tyrosine kinase is activated in the cellular responses to genotoxic, oxidative and other forms of stress. Using tagged forms of c-Abl, the present studies demonstrate that c-Abl forms homodimers in cells. The results show that the c-Abl N-terminal regions interact with the corresponding C-terminal regions of both partners in the dimmer. Specifically, the c-Abl SH3 domain binds to a proline-rich motif at amino acids 958-982 in the c-Abl C-terminal region. Deletion of the prolinerich motif disrupts dimmer formation. These findings provide the first evidence that c-Abl forms homodimers and indicate that homodimerization can contribute to the regulation of c-Abl activity.%c-Abl是非受体酪氨酸激酶,它在细胞内被一些基因毒性的、氧化的及其它形式的压力所激活.目前研究证明:应用标记的c-Abl发现其在细胞内可以相互形成同源二聚体,并且一分子c-Abl的N末端区域与相应的另一分子的C末端相互作用形成二聚体.实验进一步表明:c-Abl SH3结构域结合到另一c-Abl分子富含脯氨酸的C-末端约958-982氨基酸区域.如果去除c-Abl富含脯氨酸的结构域,就会阻止二聚体的形成.这些结果首先证实了c-Abl在细胞内可以相互形成同源二聚体,并暗示着二聚体的形成可能影响着c-Abl活性的调节.
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